{
  "abstract": "The SARS-CoV-2 Spike (S) glycoprotein, which plays a central role in viral entry, consists of two subunits: S1, which mediates binding to the ACE2 receptor; and S2, which induces fusion of the viral envelope with the cell membrane. The S glycoprotein also contains a polybasic motif at the S1/S2 junction that is recognised by the furin-type protease family, modulating its entry functions. Several of the 22 N-glycans that decorate S are located near the S1/S2 boundary and are likely to influence S cleavage, which is crucial for inducing fusiona key step in viral entry. This study characterised the importance of the N-glycans N603, N616, and N657 for S cleavage and its ability to induce fusion and entry. Our data revealed that S harbouring mutations at these three sites relies on a basic residue at position 634 for cleavage. Furthermore, while these N-glycans and R634 were necessary for the ability of S to mediate fusion and entry in the G614 and D614 variants, mutations in these residues had a milder impact in the XBB.1.5 Omicron variant. Consequently, the roles of N603, N616, N657 and R634 in S cleavage, fusion induction and viral entry have evolved alongside these different variants.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 5,
  "authors": [
    {
      "name": "Muriel Lavie"
    },
    {
      "name": "Emma Louvet"
    },
    {
      "name": "Jules Patron"
    },
    {
      "name": "Xavier Hanoulle"
    },
    {
      "name": "Sandrine Belouzard"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/f6en01y1fvwfj.bib",
  "cited_by": 0,
  "doi": "10.1038/s41598-026-70382-z",
  "fulltext_url": null,
  "id": "f6en01y1fvwfj",
  "issns": [
    "2045-2322"
  ],
  "landing_url": "https://hal.science/hal-05786192v1",
  "language": "en",
  "licence": "CC-BY-NC-ND-4.0",
  "licence_label": "CC BY-NC-ND 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.sdv"
    ],
    [
      "hal",
      "1.sdv.bbm"
    ],
    [
      "hal",
      "1.sdv.mhep"
    ],
    [
      "hal",
      "1.sdv.mp"
    ],
    [
      "hal",
      "2.sdv.bbm.gtp"
    ],
    [
      "hal",
      "2.sdv.mhep.me"
    ],
    [
      "hal",
      "2.sdv.mhep.mi"
    ],
    [
      "hal",
      "2.sdv.mp.vir"
    ],
    [
      "openalex",
      "2725|SARS-CoV-2 and COVID-19 Research"
    ]
  ],
  "openalex": "W7212355100",
  "pdf_url": "https://hal.science/hal-05786192/document",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-12",
  "publisher": "Nature Publishing Group",
  "ris": "https://research.draconitic.com/paper/f6en01y1fvwfj.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:50Z",
      "native_id": "hal-05786192",
      "source": "hal",
      "url": "https://hal.science/hal-05786192v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "hal:2.sdv.bbm.gtp",
      "subfield": "proteomics-metabolomics"
    },
    {
      "field": "biology",
      "origin": "hal:1.sdv.mp",
      "subfield": "microbiology"
    },
    {
      "field": "medicine",
      "origin": "hal:2.sdv.mhep.me",
      "subfield": "infectious-disease"
    }
  ],
  "title": "Glycans located upstream of the furin cleavage site in SARS-CoV-2 Spike protein influence its processing and functions",
  "title_text": "Glycans located upstream of the furin cleavage site in SARS-CoV-2 Spike protein influence its processing and functions",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:50Z",
  "url": "https://research.draconitic.com/paper/f6en01y1fvwfj",
  "venue": "Scientific Reports",
  "versions": []
}